2.02012-05-31 10:23:25 -06002015-09-13 12:56:06 -0600ECMDB00191M2MDB000080L-Aspartic acidAspartic acid (Asp, D), also known as aspartate (the name of its anion), is one of the 20 natural proteinogenic amino acids which are the building blocks of proteins. Aspartic acid has 2 enantiomeric forms: D and L. L-aspartic acid is the isomer with more biological roles and is the form used in constructing proteins. (Wikipedia) In E. coli, L-aspartate can be produced from L-glutamate, and interconversion can occur between L-asparagine and L-aspartate. L-aspartate is also involved in the biosynthesis pathways of many compounds, including adenosine nucleotides, beta-alanine, and homoserine. (EcoCyc)(+)-Aspartate(+)-Aspartic acid(2S)-Aspartate(2S)-Aspartic acid(L)-Aspartate(L)-Aspartic acid(R)-2-aminosuccinate(R)-2-aminosuccinic acid(S)-(+)-Aspartate(S)-(+)-Aspartic acid(S)-2-aminosuccinate(S)-2-aminosuccinic acid(S)-amino-Butanedioate(S)-amino-Butanedioic acid(S)-Aminobutanedioate(S)-Aminobutanedioic acid(S)-Aspartate(S)-Aspartic acid2-Amino-3-methylsuccinate2-Amino-3-methylsuccinic acid2-Aminosuccinate2-Aminosuccinic acida-Aminosuccinatea-Aminosuccinic acidAlpha-AminosuccinateAlpha-Aminosuccinic acidAminosuccinateAminosuccinic acidAspAsparagateAsparagic acidAsparaginateAsparaginic acidAsparatateAsparatic acidAspartateAspartic acidDH-Asp-OHL-(+)-AspartateL-(+)-Aspartic acidL-AminosuccinateL-Aminosuccinic acidL-AsparagateL-Asparagic acidL-AsparaginateL-Asparaginic acidL-AspartateL-aspartic acidα-Aminosuccinateα-Aminosuccinic acidC4H7NO4133.1027133.037507717(2S)-2-aminobutanedioic acidL-aspartic acid56-84-8N[C@@H](CC(O)=O)C(O)=OInChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m0/s1CKLJMWTZIZZHCS-REOHCLBHSA-NSolidCytosolExtra-organismPeriplasmlogp-3.52logs0.03solubility1.42e+02 g/lmelting_point270 oClogp-3.5pka_strongest_acidic1.7pka_strongest_basic9.61iupac(2S)-2-aminobutanedioic acidaverage_mass133.1027mono_mass133.037507717smilesN[C@@H](CC(O)=O)C(O)=OformulaC4H7NO4inchiInChI=1S/C4H7NO4/c5-2(4(8)9)1-3(6)7/h2H,1,5H2,(H,6,7)(H,8,9)/t2-/m0/s1inchikeyCKLJMWTZIZZHCS-REOHCLBHSA-Npolar_surface_area100.62refractivity26.53polarizability11.28rotatable_bond_count3acceptor_count5donor_count3physiological_charge-1formal_charge0Alanine, aspartate and glutamate metabolismec00250Arginine and proline metabolismec00330Nitrogen metabolism
The biological process of the nitrogen cycle is a complex interplay among many microorganisms catalyzing different reactions, where nitrogen is found in various oxidation states ranging from +5 in nitrate to -3 in ammonia.
The ability of fixing atmospheric nitrogen by the nitrogenase enzyme complex is present in restricted prokaryotes (diazotrophs). The other reduction pathways are assimilatory nitrate reduction and dissimilatory nitrate reduction both for conversion to ammonia, and denitrification. Denitrification is a respiration in which nitrate or nitrite is reduced as a terminal electron acceptor under low oxygen or anoxic conditions, producing gaseous nitrogen compounds (N2, NO and N2O) to the atmosphere.
Nitrate can be introduced into the cytoplasm through a nitrate:nitrite antiporter NarK or a nitrate / nitrite transporter NarU. Nitrate is then reduced by a Nitrate Reductase resulting in the release of water, an acceptor and a Nitrite. Nitrite can also be introduced into the cytoplasm through a nitrate:nitrite antiporter NarK
Nitrite can be reduced a NADPH dependent nitrite reductase resulting in water and NAD and Ammonia.
Nitrite can interact with hydrogen ion, ferrocytochrome c through a cytochrome c-552 ferricytochrome resulting in the release of ferricytochrome c, water and ammonia
Another process by which ammonia is produced is by a reversible reaction of hydroxylamine with a reduced acceptor through a hydroxylamine reductase resulting in an acceptor, water and ammonia.
Water and carbon dioxide react through a carbonate dehydratase resulting in carbamic acid. This compound reacts spontaneously with hydrogen ion resulting in the release of carbon dioxide and ammonia. Carbon dioxide can interact with water through a carbonic anhydrase resulting in hydrogen carbonate. This compound interacts with cyanate and hydrogen ion through a cyanate hydratase resulting in a carbamic acid.
Ammonia can be metabolized by reacting with L-glutamine and ATP driven glutamine synthetase resulting in ADP, phosphate and L-glutamine. The latter compound reacts with oxoglutaric acid and hydrogen ion through a NADPH dependent glutamate synthase resulting in the release of NADP and L-glutamic acid. L-glutamic acid reacts with water through a NADP-specific glutamate dehydrogenase resulting in the release of oxoglutaric acid, NADPH, hydrogen ion and ammonia.
PW000755ec00910MetabolicPurine metabolismec00230Pyrimidine metabolismThe metabolism of pyrimidines begins with L-glutamine interacting with water molecule and a hydrogen carbonate through an ATP driven carbamoyl phosphate synthetase resulting in a hydrogen ion, an ADP, a phosphate, an L-glutamic acid and a carbamoyl phosphate. The latter compound interacts with an L-aspartic acid through a aspartate transcarbamylase resulting in a phosphate, a hydrogen ion and a N-carbamoyl-L-aspartate. The latter compound interacts with a hydrogen ion through a dihydroorotase resulting in the release of a water molecule and a 4,5-dihydroorotic acid. This compound interacts with an ubiquinone-1 through a dihydroorotate dehydrogenase, type 2 resulting in a release of an ubiquinol-1 and an orotic acid. The orotic acid then interacts with a phosphoribosyl pyrophosphate through a orotate phosphoribosyltransferase resulting in a pyrophosphate and an orotidylic acid. The latter compound then interacts with a hydrogen ion through an orotidine-5 '-phosphate decarboxylase, resulting in an release of carbon dioxide and an Uridine 5' monophosphate. The Uridine 5' monophosphate process to get phosphorylated by an ATP driven UMP kinase resulting in the release of an ADP and an Uridine 5--diphosphate.
Uridine 5-diphosphate can be metabolized in multiple ways in order to produce a Deoxyuridine triphosphate.
1.-Uridine 5-diphosphate interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in the release of a water molecule and an oxidized thioredoxin and an dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate.
2.-Uridine 5-diphosphate interacts with a reduced NrdH glutaredoxin-like protein through a Ribonucleoside-diphosphate reductase 1 resulting in a release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dUDP. The dUDP is then phosphorylated by an ATP through a nucleoside diphosphate kinase resulting in the release of an ADP and a DeoxyUridine triphosphate.
3.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate. The latter compound interacts with a reduced flavodoxin through ribonucleoside-triphosphate reductase resulting in the release of an oxidized flavodoxin, a water molecule and a Deoxyuridine triphosphate
4.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in the release of a water molecule, an oxidized flavodoxin and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate.
5.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP then interacts with a reduced NrdH glutaredoxin-like protein through a ribonucleoside-diphosphate reductase 2 resulting in the release of a water molecule, an oxidized NrdH glutaredoxin-like protein and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate.
6.-Uridine 5-diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and an Uridinetriphosphate The uridine triphosphate interacts with a L-glutamine and a water molecule through an ATP driven CTP synthase resulting in an ADP, a phosphate, a hydrogen ion, an L-glutamic acid and a cytidine triphosphate. The cytidine triphosphate then interacts spontaneously with a water molecule resulting in the release of a phosphate, a hydrogen ion and a CDP. The CDP interacts with a reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dCDP. The dCDP is then phosphorylated through an ATP driven nucleoside diphosphate kinase resulting in an ADP and a dCTP. The dCTP interacts with a water molecule and a hydrogen ion through a dCTP deaminase resulting in a release of an ammonium molecule and a Deoxyuridine triphosphate.
The deoxyuridine triphosphate then interacts with a water molecule through a nucleoside triphosphate pyrophosphohydrolase resulting in a release of a hydrogen ion, a phosphate and a dUMP. The dUMP then interacts with a methenyltetrahydrofolate through a thymidylate synthase resulting in a dihydrofolic acid and a 5-thymidylic acid. Then 5-thymidylic acid is then phosphorylated through a nucleoside diphosphate kinase resulting in the release of an ADP and thymidine 5'-triphosphate.PW000942ec00240MetabolicCysteine and methionine metabolismec00270Tyrosine metabolismec00350Phenylalanine metabolismThe pathways of the metabolism of phenylalaline begins with the conversion of chorismate to prephenate through a P-protein (chorismate mutase:pheA). Prephenate then interacts with a hydrogen ion through the same previous enzyme resulting in a release of carbon dioxide, water and a phenolpyruvic acid. Three enzymes those enconde by tyrB, aspC and ilvE are involved in catalyzing the third step of these pathways, all three can contribute to the synthesis of phenylalanine: only tyrB and aspC contribute to biosynthesis of tyrosine.
Phenolpyruvic acid can also be obtained from a reversivle reaction with ammonia, a reduced acceptor and a D-amino acid dehydrogenase, resulting in a water, an acceptor and a D-phenylalanine, which can be then transported into the periplasmic space by aromatic amino acid exporter.
L-phenylalanine also interacts in two reversible reactions, one involved with oxygen through a catalase peroxidase resulting in a carbon dioxide and 2-phenylacetamide. The other reaction involved an interaction with oxygen through a phenylalanine aminotransferase resulting in a oxoglutaric acid and phenylpyruvic acid.
L-phenylalanine can be imported into the cytoplasm through an aromatic amino acid:H+ symporter AroP.
The compound can also be imported into the periplasmic space through a transporter: L-amino acid efflux transporter.PW000921ec00360MetabolicPhenylalanine, tyrosine and tryptophan biosynthesisec00400Novobiocin biosynthesisec00401Carbon fixation in photosynthetic organismsec00710Isoquinoline alkaloid biosynthesisec00950Tropane, piperidine and pyridine alkaloid biosynthesisec00960Glycine, serine and threonine metabolismec00260Lysine biosynthesisLysine is biosynthesized from L-aspartic acid. L-aspartic acid can be incorporated into the cell through various methods: C4 dicarboxylate / orotate:H+ symporter ,
glutamate / aspartate : H+ symporter GltP, dicarboxylate transporter , C4 dicarboxylate / C4 monocarboxylate transporter DauA, glutamate / aspartate ABC transporter
L-aspartic acid is phosphorylated by an ATP-driven Aspartate kinase resulting in ADP and L-aspartyl-4-phosphate. L-aspartyl-4-phosphate is then dehydrogenated through an NADPH driven aspartate semialdehyde dehydrogenase resulting in a release of phosphate, NADP and L-aspartic 4-semialdehyde (involved in methionine biosynthesis).
L-aspartic 4-semialdehyde interacts with a pyruvic acid through a 4-hydroxy-tetrahydrodipicolinate synthase resulting in a release of hydrogen ion, water and
(2S,4S)-4-hydroxy-2,3,4,5-tetrahydrodipicolinate. The latter compound is then reduced by an NADPH driven 4-hydroxy-tetrahydrodipicolinate reductase resulting in a release of water, NADP and (S)-2,3,4,5-tetrahydrodipicolinate, This compound interacts with succinyl-CoA and water through a tetrahydrodipicolinate succinylase resulting in a release of coenzyme A and N-Succinyl-2-amino-6-ketopimelate. This compound interacts with L-glutamic acid through a N-succinyldiaminopimelate aminotransferase resulting in oxoglutaric acid, N-succinyl-L,L-2,6-diaminopimelate. The latter compound is then desuccinylated by reacting with water through a N-succinyl-L-diaminopimelate desuccinylase resulting in a succinic acid and L,L-diaminopimelate. This compound is then isomerized through a diaminopimelate epimerase resulting in a meso-diaminopimelate (involved in peptidoglyccan biosynthesis I). This compound is then decarboxylated by a diaminopimelate decarboxylase resulting in a release of carbon dioxide and L-lysine.
L-lysine is then incorporated into lysine degradation pathway. Lysine also regulate its own biosynthesis by repressing dihydrodipicolinate synthase and also repressing lysine-sensitive aspartokinase 3.
A metabolic connection joins synthesis of an amino acid, lysine, to synthesis of cell wall material. Diaminopimelate is a precursor both for lysine and for cell wall components. The synthesis of lysine, methionine and threonine share two reactions at the start of the three pathways, the reactions converting L-aspartate to L-aspartate semialdehyde. The reaction involving aspartate kinase is carried out by three isozymes, one specific for synthesis of each end product amino acid. Each of the three aspartate kinase isozymes is regulated by its corresponding end product amino acid.PW000771ec00300MetabolicCyanoamino acid metabolismec00460Pantothenate and CoA biosynthesisThe CoA biosynthesis requires compounds from two other pathways: aspartate metabolism and valine biosynthesis. It requires a Beta-Alanine and R-pantoate.
The compound (R)-pantoate is generated in two reactions, as shown by the interaction of alpha-ketoisovaleric acid, 5,10 methylene-THF and water through a 3-methyl-2-oxobutanoate hydroxymethyltransferase resulting in a tetrahydrofolic acid and a 2-dehydropantoate. This compound interacts with hydrogen through a NADPH driven acetohydroxy acid isomeroreductase resulting in the release of NADP and R-pantoate.
On the other hand L-aspartic acid interacts with a hydrogen ion and gets decarboxylated through an Aspartate 1- decarboxylase resulting in a carbon dioxide and a Beta-alanine.
Beta-alanine and R-pantoate interact with an ATP driven pantothenate synthetase resulting in pyrophosphate, AMP, hydrogen ion and pantothenic acid.
Pantothenic acid is phosphorylated through a ATP-driven pantothenate kinase resulting in a ADP, a hydrogen ion and D-4'-Phosphopantothenate. This compound interacts with a CTP and a L-cysteine resulting in a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a hydrogen ion, a pyrophosphate, a CMP and 4-phosphopantothenoylcysteine.
The latter compound interacts with a hydrogen ion through a fused 4'-phosphopantothenoylcysteine decarboxylase and phosphopantothenoylcysteine synthetase resulting in a carbon dioxide release and a 4-phosphopantetheine. This compound interacts with an ATP, hydrogen ion and an phosphopantetheine adenylyltransferase resulting in a release of pyrophosphate, and dephospho-CoA.
Dephospho-CoA reacts with an ATP driven dephospho-CoA kinase resulting in a ADP , a hydrogen ion and a Coenzyme A.
. The latter is converted into (R)-4'-phosphopantothenate is two steps, involving a β-alanine ligase and a kinase. In most organsims the ligase acts before the kinase (EC 6.3.2.1, pantoate—β-alanine ligase (AMP-forming) followed by EC 2.7.1.33, pantothenate kinase, as described in phosphopantothenate biosynthesis I and phosphopantothenate biosynthesis II. However, in archaea the order is reversed, and EC 2.7.1.169, pantoate kinase acts before EC 6.3.2.36, 4-phosphopantoate—β-alanine ligase, as described in phosphopantothenate biosynthesis III.
The kinases are feedback inhibited by CoA itself, accounting for the primary regulatory mechanism of CoA biosynthesis. The addition of L-cysteine to (R)-4'-phosphopantothenate, resulting in the formation of R-4'-phosphopantothenoyl-L-cysteine (PPC), is followed by decarboxylation of PPC to 4'-phosphopantetheine. The ultimate reaction is catalyzed by EC 2.7.1.24, dephospho-CoA kinase, which converts 4'-phosphopantetheine to CoA. All enzymes of this pathway are essential for growth.
The reactions in the biosynthetic route towards CoA are identical in most organisms, although there are differences in the functionality of the involved enzymes. In plants every step is catalyzed by single monofunctional enzymes, whereas in bacteria and mammals bifunctional enzymes are often employed [Rubio06].PW000828ec00770MetabolicAminoacyl-tRNA biosynthesisec00970Histidine metabolismec00340Nicotinate and nicotinamide metabolismec00760beta-Alanine metabolismThe Beta-Alanine Metabolism starts with a product of Aspartate metabolism. Aspartate is decarboxylated by aspartate 1-decarboxylase, releasing carbon dioxide and Beta-alanine. Beta alanine is then metabolized through a pantothenate synthetase resulting in Pantothenic acid undergoes phosphorylation through a ATP driven pantothenate kinase, resulting in D-4-phosphopantothenate.
Pantothenate (vitamin B5) is the universal precursor for the synthesis of the 4'-phosphopantetheine moiety of coenzyme A and acyl carrier protein. Only plants and microorganismscan synthesize pantothenate de novo - animals require a dietary supplement. The enzymes of this pathway are therefore considered to be antimicrobial drug targets.PW000896ec00410MetabolicMicrobial metabolism in diverse environmentsec01120ABC transportersec02010Two-component systemec02020Bacterial chemotaxisec02030Monobactam biosynthesiseco00261Metabolic pathwayseco01100Asparagine biosynthesisL-asparagine is synthesized in E. coli from L-aspartate by either of two reactions, utilizing either L-glutamine or ammonia as the amino group donor. Both reactions are ATP driven and yield AMP and pyrophosphate.
The first reaction is catalyzed only by asparagine synthetase B, while the second reaction is catalyzed by both asparagine synthetase A and asparagine synthetase B,
The only known role of asparagine in the metabolism of E. coli is as a constituent of protein. PW000813MetabolicAspartate metabolismAspartate (seen in the center) is synthesized from and degraded to oxaloacetate , an intermediate of the TCA cycle, by a reversible transamination reaction with glutamate. As shown here, AspC is the principal transaminase that catalyzes this reaction, but TyrB also catalyzes it. Null mutations in aspC do not confer aspartate auxotrophy; null mutations in both aspC and tyrB do.
Aspartate is a constituent of proteins and participates in several other biosyntheses as shown here( NAD biosynthesis and Beta-Alanine Metabolism . Approximately 27 percent of the cell's nitrogen flows through aspartate
Aspartate can be synthesized from fumaric acid through a aspartate ammonia lyase. Aspartate also participates in the synthesis of L-asparagine through two different methods, either through aspartate ammonia ligase or asparagine synthetase B.
Aspartate is also a precursor of fumaric acid. Again it has two possible ways of synthesizing it. First set of reactions follows an adenylo succinate synthetase that yields adenylsuccinic acid and then adenylosuccinate lyase in turns leads to fumaric acid. The second way is through argininosuccinate synthase that yields argininosuccinic acid and then argininosuccinate lyase in turns leads to fumaric acid
PW000787MetabolicL-glutamate metabolism
There are various ways by which glutamate enters the cytoplasm in E.coli. through a glutamate:sodium symporter, glutamate / aspartate : H+ symporter GltP or a
glutamate / aspartate ABC transporter.
There are various ways by which E. coli synthesizes glutamate from L-glutamine or oxoglutaric acid.
L-glutamine, introduced into the cytoplasm by glutamine ABC transporter, can either interact with glutaminase resulting in ammonia and L-glutamic acid, or react with oxoglutaric acid, and hydrogen ion through an NADPH driven glutamate synthase resulting in L-glutamic acid.
L-glutamic acid is metabolized into L-glutamine by reacting with ammonium through a ATP driven glutamine synthase. L-glutamic acid can also be metabolized into L-aspartic acid by reacting with oxalacetic acid through an aspartate transaminase resulting in n oxoglutaric acid and L-aspartic acid. L-aspartic acid is metabolized into fumaric acid through an
aspartate ammonia-lyase. Fumaric acid can be introduced into the cytoplasm through 3 methods:
dicarboxylate transporter , C4 dicarboxylate / C4 monocarboxylate transporter DauA, and C4 dicarboxylate / orotate:H+ symporter
PW000789MetabolicNAD biosynthesisNicotinamide adenine dinucleotide (NAD) can be biosynthesized from L-aspartic acid.This amino acid reacts with oxygen through an L-aspartate oxidase resulting in a hydrogen ion, hydrogen peroxide and an iminoaspartic acid. The latter compound interacts with dihydroxyacetone phosphate through a quinolinate synthase A, resulting in a phosphate, water, and a quinolic acid. Quinolic acid interacts with phosphoribosyl pyrophosphate and hydrogen ion through a quinolinate phosphoribosyltransferase resulting in pyrophosphate, carbon dioxide and nicotinate beta-D-ribonucleotide. This last compound is adenylated through an ATP driven nicotinate-mononucleotide adenylyltransferase releasing a pyrophosphate and resulting in a nicotinic acid adenine dinucleotide.
Nicotinic acid adenine dinucleotide is processed through an NAD synthetase, NH3-dependent in two different manners.
In the first case, Nicotinic acid adenine dinucleotide interacts with ATP, L-glutamine and water through the enzyme and results in hydrogen ion, AMP, pyrophosphate, L-glutamic acid and NAD.
In the second case, Nicotinic acid adenine dinucleotide interacts with ATP and ammonium through the enzyme resulting in a pyrophosphate, AMP, hydrogen ion and NAD.
NAD then proceeds to regulate its own pathway by repressing L-aspartate oxidase.
As a general rule, most prokaryotes utilize the aspartate de novo pathway, in which the nicotinate moiety of NAD is synthesized from aspartate , while in eukaryotes, the de novo pathway starts with tryptophan.
PW000829MetabolicSecondary Metabolites: threonine biosynthesis from aspartateThe biosynthesis of threonine starts with L-aspartic acid being phosphorylated by an ATP driven Aspartate kinase resulting in an a release of an ADP and an L-aspartyl-4-phosphate. This compound interacts with a hydrogen ion through an NADPH driven aspartate semialdehyde dehydrogenase resulting in the release of a phosphate, an NADP and a L-aspartate-semialdehyde.The latter compound interacts with a hydrogen ion through a NADPH driven aspartate kinase / homoserine dehydrogenase resulting in the release of an NADP and a L-homoserine. L-homoserine is phosphorylated through an ATP driven homoserine kinase resulting in the release of an ADP, a hydrogen ion and a O-phosphohomoserine. The latter compound then interacts with a water molecule threonine synthase resulting in the release of a phosphate and an L-threonine. PW000976Metabolicarginine metabolismThe metabolism of L-arginine starts with the acetylation of L-glutamic acid resulting in a N-acetylglutamic acid while releasing a coenzyme A and a hydrogen ion. N-acetylglutamic acid is then phosphorylated via an ATP driven acetylglutamate kinase which yields a N-acetyl-L-glutamyl 5-phosphate. This compound undergoes a NDPH dependent reduction resulting in N-acetyl-L-glutamate 5-semialdehyde. This compound reacts with L-glutamic acid through a acetylornithine aminotransferase / N-succinyldiaminopimelate aminotransferase to produce a N-acetylornithine which is then deacetylated through a acetylornithine deacetylase which yield an ornithine.
L-glutamine is used to synthesize carbamoyl phosphate through the interaction of L-glutamine, water, ATP, and hydrogen carbonate. This reaction yields ADP, L-glutamic acid, phosphate, and hydrogen ion.
Carbamoyl phosphate and ornithine are used to catalyze the production of citrulline through an ornithine carbamoyltransferase. Citrulline reacts with L-aspartic acid through an ATP dependent enzyme, argininosuccinate synthase to produce pyrophosphate, AMP and argininosuccinic acid. Argininosussinic acid is then lyase to produce L-arginine and fumaric acid.
L-arginine can be metabolized into succinic acid by two different sets of reactions:
1. Arginine reacts with succinyl-CoA through a arginine N-succinyltransferase resulting in N2-succinyl-L-arginine while releasing CoA and Hydrogen Ion. N2-succinyl-L-arginine is then dihydrolase to produce a N2-succinyl-L-ornithine through a N-succinylarginine dihydrolase. This compound in turn reacts with oxoglutaric acid through succinylornithine transaminase resulting in L-glutamic acid and N2-succinyl-L-glutamic acid 5-semialdehyde. This compoud in turn reacts with a NAD dependent dehydrogenase resulting in N2-succinylglutamate while releasing NADH and hydrogen ion. N2-succinylglutamate reacts with water through a succinylglutamate desuccinylase resulting in L-glutamic acid and
a succinic acid. The succinic acid is then incorporated in the TCA cycle
2.Argine reacts with carbon dioxide and a hydrogen ion through a biodegradative arginine decarboxylase, resulting in Agmatine. This compound is then transformed into putrescine by reacting with water and an agmatinase, and releasing urea. Putrescine can be metabolized by reaction with either l-glutamic acid or oxoglutaric acid. If putrescine reacts with L-glutamic acid, it reacts through an ATP mediated gamma-glutamylputrescine producing a hydrogen ion, ADP, phosphate and gamma-glutamyl-L-putrescine. This compound is reduced by interacting with oxygen, water and a gamma-glutamylputrescine oxidoreductase resulting in ammonium, hydrogen peroxide and 4-gamma-glutamylamino butanal. This compound is dehydrogenated through a NADP mediated reaction lead by gamma-glutamyl-gamma-aminobutaryaldehyde dehydrogenase resulting in hydrogen ion, NADPH and 4-glutamylamino butanoate. In turn, the latter compound reacts with water through a gamma-glutamyl-gamma-aminobutyrate hydrolase resulting in L-glutamic acid and Gamma aminobutyric acid. On the other hand, if putrescine reacts with oxoglutaric acid through a putrescine aminotransferase, it results in L-glutamic acid, and a 4-aminobutyraldehyde. This compound reacts with water through a NAD dependent gamma aminobutyraldehyde dehydrogenase resulting in hydrogen ion, NADH and gamma-aminobutyric acid.
Gamma Aaminobutyric acid reacts with oxoglutaric acid through 4-aminobutyrate aminotransferase resulting in L-glutamic acid and succinic acid semialdehyde. This compound in turn can react with with either NADP or NAD to result in the production of succinic acid through succinate-semialdehyde dehydrogenase or aldehyde dehydrogenase-like protein yneI respectively. Succinic acid can then be integrated in the TCA cycle.
L-arginine is eventua lly metabolized into succinic acid which then goes to the TCA cyclePW000790Metabolicpurine nucleotides de novo biosynthesisThe biosynthesis of purine nucleotides is a complex process that begins with a phosphoribosyl pyrophosphate. This compound interacts with water and L-glutamine through a
amidophosphoribosyl transferase resulting in a pyrophosphate, L-glutamic acid and a 5-phosphoribosylamine. The latter compound proceeds to interact with a glycine through an ATP driven phosphoribosylamine-glycine ligase resulting in the addition of glycine to the compound. This reaction releases an ADP, a phosphate, a hydrogen ion and a N1-(5-phospho-β-D-ribosyl)glycinamide. The latter compound interacts with formic acid, through an ATP driven phosphoribosylglycinamide formyltransferase 2 resulting in a phosphate, an ADP, a hydrogen ion and a 5-phosphoribosyl-N-formylglycinamide. The latter compound interacts with L-glutamine, and water through an ATP-driven
phosphoribosylformylglycinamide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion, a L-glutamic acid and a 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine. The latter compound interacts with an ATP driven phosphoribosylformylglycinamide cyclo-ligase resulting in a release of ADP, a phosphate, a hydrogen ion and a 5-aminoimidazole ribonucleotide. The latter compound interacts with a hydrogen carbonate through an ATP driven N5-carboxyaminoimidazole ribonucleotide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion and a N5-carboxyaminoimidazole ribonucleotide.The latter compound then interacts with a N5-carboxyaminoimidazole ribonucleotide mutase resulting in a 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. This compound interacts with an L-aspartic acid through an ATP driven phosphoribosylaminoimidazole-succinocarboxamide synthase resulting in a phosphate, an ADP, a hydrogen ion and a SAICAR. SAICAR interacts with an adenylosuccinate lyase resulting in a fumaric acid and an AICAR. AICAR interacts with a formyltetrahydrofolate through a AICAR transformylase / IMP cyclohydrolase resulting in a release of a tetrahydropterol mono-l-glutamate and a FAICAR. The latter compound, FAICAR, interacts in a reversible reaction through a AICAR transformylase / IMP cyclohydrolase resulting in a release of water and Inosinic acid.
Inosinic acid can be metabolized to produce dGTP and dATP three different methods each.
dGTP:
Inosinic acid, water and NAD are processed by IMP dehydrogenase resulting in a release of NADH, a hydrogen ion and Xanthylic acid. Xanthylic acid interacts with L-glutamine, and water through an ATP driven GMP synthetase resulting in pyrophosphate, AMP, L-glutamic acid, a hydrogen ion and Guanosine monophosphate. The latter compound is the phosphorylated by reacting with an ATP driven guanylate kinase resulting in a release of ADP and a Gaunosine diphosphate. Guanosine diphosphate can be metabolized in three different ways:
1.-Guanosine diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and a Guanosine triphosphate. This compound interacts with a reduced flavodoxin protein through a ribonucleoside-triphosphate reductase resulting in a oxidized flavodoxin a water moleculer and a dGTP
2.-Guanosine diphosphate interacts with a reduced NrdH glutaredoxin-like proteins through a ribonucleoside-diphosphate reductase 2 resulting in the release of an oxidized NrdH glutaredoxin-like protein, a water molecule and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP.
3.-Guanosine diphosphate interacts with a reduced thioredoxin ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP.
dATP:
Inosinic acid interacts with L-aspartic acid through an GTP driven adenylosuccinate synthase results in the release of GDP, a hydrogen ion, a phosphate and N(6)-(1,2-dicarboxyethyl)AMP. The latter compound is then cleaved by a adenylosuccinate lyase resulting in a fumaric acid and an Adenosine monophosphate. This compound is then phosphorylated by an adenylate kinase resulting in the release of ATP and an adenosine diphosphate. Adenosine diphosphate can be metabolized in three different ways:
1.-Adenosine diphosphate is involved in a reversible reaction by interacting with a hydrogen ion and a phosphate through a ATP synthase / thiamin triphosphate synthase resulting in a hydrogen ion, a water molecule and an Adenosine triphosphate. The adenosine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in an oxidized flavodoxin, a water molecule and a dATP
2.- Adenosine diphosphate interacts with an reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, a oxidized thioredoxin and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP
3.- Adenosine diphosphate interacts with an reduced NrdH glutaredoxin-like protein through a ribonucleoside diphosphate reductase 2 resulting in a release of a water molecule, a oxidized glutaredoxin-like protein and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP
PW000910Metabolicpurine nucleotides de novo biosynthesis 1435709748PW000960MetabolictRNA Charging 2This pathway groups together all E. coli tRNA charging reactions.PW000803MetabolictRNA chargingThis pathway groups together all E. coli tRNA charging reactions.PW000799Metabolicthreonine biosynthesisThe biosynthesis of threonine starts with oxalacetic acid interacting with an L-glutamic acid through an aspartate aminotransferase resulting in a oxoglutaric acid and an L-aspartic acid. The latter compound is then phosphorylated by an ATP driven Aspartate kinase resulting in an a release of an ADP and an L-aspartyl-4-phosphate. This compound interacts with a hydrogen ion through an NADPH driven aspartate semialdehyde dehydrogenase resulting in the release of a phosphate, an NADP and a L-aspartate-semialdehyde.The latter compound interacts with a hydrogen ion through a NADPH driven aspartate kinase / homoserine dehydrogenase resulting in the release of an NADP and a L-homoserine. L-homoserine is phosphorylated through an ATP driven homoserine kinase resulting in the release of an ADP, a hydrogen ion and a O-phosphohomoserine. The latter compound then interacts with a water molecule threonine synthase resulting in the release of a phosphate and an L-threonine. PW000817Metabolicpurine nucleotides de novo biosynthesis 2The biosynthesis of purine nucleotides is a complex process that begins with a phosphoribosyl pyrophosphate. This compound interacts with water and L-glutamine through a amidophosphoribosyl transferase resulting in a pyrophosphate, L-glutamic acid and a 5-phosphoribosylamine. The latter compound proceeds to interact with a glycine through an ATP driven phosphoribosylamine-glycine ligase resulting in the addition of glycine to the compound. This reaction releases an ADP, a phosphate, a hydrogen ion and a N1-(5-phospho-β-D-ribosyl)glycinamide. The latter compound interacts with formic acid, through an ATP driven phosphoribosylglycinamide formyltransferase 2 resulting in a phosphate, an ADP, a hydrogen ion and a 5-phosphoribosyl-N-formylglycinamide. The latter compound interacts with L-glutamine, and water through an ATP-driven phosphoribosylformylglycinamide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion, a L-glutamic acid and a 2-(formamido)-N1-(5-phospho-D-ribosyl)acetamidine. The latter compound interacts with an ATP driven phosphoribosylformylglycinamide cyclo-ligase resulting in a release of ADP, a phosphate, a hydrogen ion and a 5-aminoimidazole ribonucleotide. The latter compound interacts with a hydrogen carbonate through an ATP driven N5-carboxyaminoimidazole ribonucleotide synthetase resulting in a release of a phosphate, an ADP, a hydrogen ion and a N5-carboxyaminoimidazole ribonucleotide(5-Phosphoribosyl-5-carboxyaminoimidazole).The latter compound then interacts with a N5-carboxyaminoimidazole ribonucleotide mutase resulting in a 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate. This compound interacts with an L-aspartic acid through an ATP driven phosphoribosylaminoimidazole-succinocarboxamide synthase resulting in a phosphate, an ADP, a hydrogen ion and a SAICAR. SAICAR interacts with an adenylosuccinate lyase resulting in a fumaric acid and an AICAR. AICAR interacts with a formyltetrahydrofolate through a AICAR transformylase / IMP cyclohydrolase resulting in a release of a tetrahydropterol mono-l-glutamate and a FAICAR. The latter compound, FAICAR, interacts in a reversible reaction through a AICAR transformylase / IMP cyclohydrolase resulting in a release of water and Inosinic acid. Inosinic acid can be metabolized to produce dGTP and dATP three different methods each. dGTP: Inosinic acid, water and NAD are processed by IMP dehydrogenase resulting in a release of NADH, a hydrogen ion and Xanthylic acid. Xanthylic acid interacts with L-glutamine, and water through an ATP driven GMP synthetase resulting in pyrophosphate, AMP, L-glutamic acid, a hydrogen ion and Guanosine monophosphate. The latter compound is the phosphorylated by reacting with an ATP driven guanylate kinase resulting in a release of ADP and a Gaunosine diphosphate. Guanosine diphosphate can be metabolized in three different ways: 1.-Guanosine diphosphate is phosphorylated by an ATP-driven nucleoside diphosphate kinase resulting in an ADP and a Guanosine triphosphate. This compound interacts with a reduced flavodoxin protein through a ribonucleoside-triphosphate reductase resulting in a oxidized flavodoxin a water moleculer and a dGTP 2.-Guanosine diphosphate interacts with a reduced NrdH glutaredoxin-like proteins through a ribonucleoside-diphosphate reductase 2 resulting in the release of an oxidized NrdH glutaredoxin-like protein, a water molecule and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. 3.-Guanosine diphosphate interacts with a reduced thioredoxin ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, an oxidized thioredoxin and a dGDP. The dGDP is then phosphorylated by interacting with an ATP-driven nucleoside diphosphate kinase resulting in an ADP and dGTP. dATP: Inosinic acid interacts with L-aspartic acid through an GTP driven adenylosuccinate synthase results in the release of GDP, a hydrogen ion, a phosphate and N(6)-(1,2-dicarboxyethyl)AMP. The latter compound is then cleaved by a adenylosuccinate lyase resulting in a fumaric acid and an Adenosine monophosphate. This compound is then phosphorylated by an adenylate kinase resulting in the release of ATP and an adenosine diphosphate. Adenosine diphosphate can be metabolized in three different ways: 1.-Adenosine diphosphate is involved in a reversible reaction by interacting with a hydrogen ion and a phosphate through a ATP synthase / thiamin triphosphate synthase resulting in a hydrogen ion, a water molecule and an Adenosine triphosphate. The adenosine triphosphate interacts with a reduced flavodoxin through a ribonucleoside-triphosphate reductase resulting in an oxidized flavodoxin, a water molecule and a dATP 2.- Adenosine diphosphate interacts with an reduced thioredoxin through a ribonucleoside diphosphate reductase 1 resulting in a release of a water molecule, a oxidized thioredoxin and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATP 3.- Adenosine diphosphate interacts with an reduced NrdH glutaredoxin-like protein through a ribonucleoside diphosphate reductase 2 resulting in a release of a water molecule, a oxidized glutaredoxin-like protein and a dADP. The dADP is then phosphorylated by a nucleoside diphosphate kinase resulting in the release of ADP and a dATPPW002033Metabolicasparagine biosynthesis IASPARAGINE-BIOSYNTHESISadenosine nucleotides <i>de novo</i> biosynthesisPWY-6126tRNA chargingTRNA-CHARGING-PWYasparagine biosynthesis IIASPARAGINESYN-PWYNAD biosynthesis I (from aspartate)PYRIDNUCSYN-PWYarginine biosynthesis IARGSYN-PWYsuperpathway of aspartate and asparagine biosynthesis; interconversion of aspartate and asparagineASPASN-PWYasparagine degradation IASPARAGINE-DEG1-PWYglutamate degradation IIGLUTDEG-PWYβ-alanine biosynthesis IIIPWY-5155uridine-5'-phosphate biosynthesisPWY-5686aspartate biosynthesisASPARTATESYN-PWYlysine biosynthesis IDAPLYSINESYN-PWYinosine-5'-phosphate biosynthesis IPWY-6123homoserine biosynthesisHOMOSERSYN-PWYSpecdb::CMs435Specdb::CMs436Specdb::CMs437Specdb::CMs438Specdb::CMs439Specdb::CMs440Specdb::CMs1130Specdb::CMs1205Specdb::CMs1395Specdb::CMs2688Specdb::CMs30054Specdb::CMs30200Specdb::CMs30303Specdb::CMs30304Specdb::CMs30305Specdb::CMs30484Specdb::CMs30733Specdb::CMs30883Specdb::CMs31058Specdb::CMs31059Specdb::CMs31060Specdb::CMs37347Specdb::CMs173357Specdb::CMs1053849Specdb::CMs1053850Specdb::NmrOneD1164Specdb::NmrOneD1199Specdb::NmrOneD4995Specdb::NmrOneD6092Specdb::NmrOneD6093Specdb::NmrOneD6094Specdb::NmrOneD6095Specdb::NmrOneD6096Specdb::NmrOneD6097Specdb::NmrOneD6098Specdb::NmrOneD6099Specdb::NmrOneD6100Specdb::NmrOneD6101Specdb::NmrOneD6102Specdb::NmrOneD6103Specdb::NmrOneD6104Specdb::NmrOneD6105Specdb::NmrOneD6106Specdb::NmrOneD6107Specdb::NmrOneD6108Specdb::NmrOneD6109Specdb::NmrOneD6110Specdb::NmrOneD6111Specdb::NmrOneD166470Specdb::MsMs304Specdb::MsMs305Specdb::MsMs306Specdb::MsMs3473Specdb::MsMs3474Specdb::MsMs3475Specdb::MsMs3476Specdb::MsMs3477Specdb::MsMs3478Specdb::MsMs3479Specdb::MsMs3480Specdb::MsMs3481Specdb::MsMs3482Specdb::MsMs3483Specdb::MsMs3484Specdb::MsMs3485Specdb::MsMs3486Specdb::MsMs3487Specdb::MsMs3488Specdb::MsMs3489Specdb::MsMs3490Specdb::MsMs3491Specdb::MsMs3492Specdb::MsMs3493Specdb::MsMs3494Specdb::NmrTwoD990Specdb::NmrTwoD1196HMDB0019159605745C0004917053L-ASPARTATEIASAspartic_acidKeseler, I. 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Obstet Gynecol. 2004 Nov;104(5 Pt 1):1011-4.15516393Bhende PM, Seaman WT, Delecluse HJ, Kenney SC: BZLF1 activation of the methylated form of the BRLF1 immediate-early promoter is regulated by BZLF1 residue 186. J Virol. 2005 Jun;79(12):7338-48.15919888Butterworth RF: Pathophysiology of hepatic encephalopathy: a new look at ammonia. Metab Brain Dis. 2002 Dec;17(4):221-7.12602499Pamfil, Maria; Lupescu, Irina; Savoiu, Valeria Gabriela. L-aspartic acid production from fumarate using Escherichia coli whole cells. Rom. (2005), 3pp. http://hmdb.ca/system/metabolites/msds/000/000/134/original/HMDB00191.pdf?1358894661Aspartate aminotransferaseP00509AAT_ECOLIaspChttp://ecmdb.ca/proteins/P00509.xmlBifunctional aspartokinase/homoserine dehydrogenase 1P00561AK1H_ECOLIthrAhttp://ecmdb.ca/proteins/P00561.xmlBifunctional aspartokinase/homoserine dehydrogenase 2P00562AK2H_ECOLImetLhttp://ecmdb.ca/proteins/P00562.xmlL-asparaginase 2P00805ASPG2_ECOLIansBhttp://ecmdb.ca/proteins/P00805.xmlAspartate--ammonia ligaseP00963ASNA_ECOLIasnAhttp://ecmdb.ca/proteins/P00963.xmlAromatic-amino-acid aminotransferaseP04693TYRB_ECOLItyrBhttp://ecmdb.ca/proteins/P04693.xmlLysine-sensitive aspartokinase 3P08660AK3_ECOLIlysChttp://ecmdb.ca/proteins/P08660.xmlArgininosuccinate synthaseP0A6E4ASSY_ECOLIargGhttp://ecmdb.ca/proteins/P0A6E4.xmlAspartate carbamoyltransferase catalytic chainP0A786PYRB_ECOLIpyrBhttp://ecmdb.ca/proteins/P0A786.xmlAspartate 1-decarboxylaseP0A790PAND_ECOLIpanDhttp://ecmdb.ca/proteins/P0A790.xmlAdenylosuccinate synthetaseP0A7D4PURA_ECOLIpurAhttp://ecmdb.ca/proteins/P0A7D4.xmlPhosphoribosylaminoimidazole-succinocarboxamide synthaseP0A7D7PUR7_ECOLIpurChttp://ecmdb.ca/proteins/P0A7D7.xmlAspartate carbamoyltransferase regulatory chainP0A7F3PYRI_ECOLIpyrIhttp://ecmdb.ca/proteins/P0A7F3.xmlL-asparaginase 1P0A962ASPG1_ECOLIansAhttp://ecmdb.ca/proteins/P0A962.xmlAspartate ammonia-lyaseP0AC38ASPA_ECOLIaspAhttp://ecmdb.ca/proteins/P0AC38.xmlL-aspartate oxidaseP10902NADB_ECOLInadBhttp://ecmdb.ca/proteins/P10902.xmlAspartyl-tRNA synthetaseP21889SYD_ECOLIaspShttp://ecmdb.ca/proteins/P21889.xmlAsparagine synthetase B [glutamine-hydrolyzing]P22106ASNB_ECOLIasnBhttp://ecmdb.ca/proteins/P22106.xmlIsoaspartyl peptidaseP37595IAAA_ECOLIiaaAhttp://ecmdb.ca/proteins/P37595.xmlGlutamate decarboxylase alphaP69908DCEA_ECOLIgadAhttp://ecmdb.ca/proteins/P69908.xmlGlutamate decarboxylase betaP69910DCEB_ECOLIgadBhttp://ecmdb.ca/proteins/P69910.xmlGlutamate/aspartate transport system permease protein gltJP0AER3GLTJ_ECOLIgltJhttp://ecmdb.ca/proteins/P0AER3.xmlGlutamate/aspartate transport system permease protein gltKP0AER5GLTK_ECOLIgltKhttp://ecmdb.ca/proteins/P0AER5.xmlGlutamate/aspartate transport ATP-binding protein gltLP0AAG3GLTL_ECOLIgltLhttp://ecmdb.ca/proteins/P0AAG3.xmlGlutamate/aspartate periplasmic-binding proteinP37902GLTI_ECOLIgltIhttp://ecmdb.ca/proteins/P37902.xmlUncharacterized amino-acid ABC transporter ATP-binding protein yecCP37774YECC_ECOLIyecChttp://ecmdb.ca/proteins/P37774.xmlInner membrane amino-acid ABC transporter permease protein yecSP0AFT2YECS_ECOLIyecShttp://ecmdb.ca/proteins/P0AFT2.xmlAnaerobic C4-dicarboxylate transporter dcuAP0ABN5DCUA_ECOLIdcuAhttp://ecmdb.ca/proteins/P0ABN5.xmlAnaerobic C4-dicarboxylate transporter dcuBP0ABN9DCUB_ECOLIdcuBhttp://ecmdb.ca/proteins/P0ABN9.xmlAnaerobic C4-dicarboxylate transporter dcuCP0ABP3DCUC_ECOLIdcuChttp://ecmdb.ca/proteins/P0ABP3.xmlGlutamate/aspartate transport system permease protein gltJP0AER3GLTJ_ECOLIgltJhttp://ecmdb.ca/proteins/P0AER3.xmlGlutamate/aspartate transport system permease protein gltKP0AER5GLTK_ECOLIgltKhttp://ecmdb.ca/proteins/P0AER5.xmlProton glutamate symport proteinP21345GLTP_ECOLIgltPhttp://ecmdb.ca/proteins/P21345.xmlOuter membrane protein NP77747OMPN_ECOLIompNhttp://ecmdb.ca/proteins/P77747.xmlOuter membrane pore protein EP02932PHOE_ECOLIphoEhttp://ecmdb.ca/proteins/P02932.xmlAerobic C4-dicarboxylate transport proteinP0A830DCTA_ECOLIdctAhttp://ecmdb.ca/proteins/P0A830.xmlGlutamate/aspartate transport ATP-binding protein gltLP0AAG3GLTL_ECOLIgltLhttp://ecmdb.ca/proteins/P0AAG3.xmlOuter membrane protein FP02931OMPF_ECOLIompFhttp://ecmdb.ca/proteins/P02931.xmlOuter membrane protein CP06996OMPC_ECOLIompChttp://ecmdb.ca/proteins/P06996.xmlGlutamate/aspartate periplasmic-binding proteinP37902GLTI_ECOLIgltIhttp://ecmdb.ca/proteins/P37902.xmlL-Aspartic acid + Carbamoylphosphate <> Ureidosuccinic acid + Hydrogen ion + PhosphateR01397ASPCARBTRANS-RXNL-Aspartic acid + Adenosine triphosphate <> L-Aspartyl-4-phosphate + ADPR00480ASPARTATEKIN-RXNAdenosine triphosphate + Water + L-Aspartic acid > ADP + L-Aspartic acid + Hydrogen ion + PhosphateTRANS-RXN0-222Adenosine triphosphate + Water + L-Aspartic acid > ADP + L-Aspartic acid + Hydrogen ion + PhosphateTRANS-RXN0-222L-Asparagine + Water > L-Aspartic acid + AmmoniumL-Aspartic acid + Hydrogen ion <> beta-Alanine + Carbon dioxideR00489ASPDECARBOX-RXNL-Aspartic acid + Adenosine triphosphate + L-Glutamine + Water > Adenosine monophosphate + L-Asparagine + L-Glutamate + Hydrogen ion + PyrophosphateR00578ASNSYNB-RXNalpha-Ketoglutarate + L-Aspartic acid <> L-Glutamate + Oxalacetic acidR00355L-Aspartic acid + Adenosine triphosphate + tRNA(Asp) + tRNA(Asp) <> Adenosine monophosphate + L-Aspartyl-tRNA(Asp) + Pyrophosphate + L-Aspartyl-tRNA(Asp)R055775-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-Aspartic acid + Adenosine triphosphate <> SAICAR + ADP + Hydrogen ion + PhosphateR04591SAICARSYN-RXNL-Aspartic acid + Fumaric acid > Hydrogen ion + Iminoaspartic acid + Succinic acidRXN-9772L-Aspartic acid + Oxygen <> Hydrogen ion + Hydrogen peroxide + Iminoaspartic acidR00481L-ASPARTATE-OXID-RXNL-Aspartic acid + Ubiquinone-8 > Hydrogen ion + Iminoaspartic acid + Ubiquinol-8L-Aspartic acid + Menaquinone 8 > Hydrogen ion + Iminoaspartic acid + Menaquinol 8L-Aspartic acid + Adenosine triphosphate + Citrulline <> Adenosine monophosphate + Argininosuccinic acid + Hydrogen ion + PyrophosphateR01954L-Aspartic acid + Adenosine triphosphate + Ammonium > Adenosine monophosphate + L-Asparagine + Hydrogen ion + PyrophosphateL-Aspartic acid > Fumaric acid + AmmoniumL-Aspartic acid + Guanosine triphosphate + Inosinic acid <> Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + PhosphateR01135L-Aspartic acid + Water + Oxygen <> Oxalacetic acid + Ammonia + Hydrogen peroxideR00357L-Aspartic acid + Oxygen <> Iminoaspartic acid + Hydrogen peroxideR00481L-ASPARTATE-OXID-RXNAdenosine triphosphate + L-Aspartic acid + Ammonia <> Adenosine monophosphate + Pyrophosphate + L-AsparagineR00483L-Asparagine + Water <> L-Aspartic acid + AmmoniaR00485L-Aspartic acid <> beta-Alanine + Carbon dioxideR00489L-Aspartic acid <> Fumaric acid + AmmoniaR00490Adenosine triphosphate + L-Aspartic acid + L-Glutamine + Water <> Adenosine monophosphate + Pyrophosphate + L-Asparagine + L-GlutamateR00578Guanosine triphosphate + Inosinic acid + L-Aspartic acid <> Guanosine diphosphate + Phosphate + Adenylsuccinic acidR01135Carbamoylphosphate + L-Aspartic acid <> Phosphate + Ureidosuccinic acidR01397Oxalacetic acid + L-Arogenate <> L-Aspartic acid + PrephenateR01731Adenosine triphosphate + Citrulline + L-Aspartic acid <> Adenosine monophosphate + Pyrophosphate + Argininosuccinic acidR01954Adenosine triphosphate + 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-Aspartic acid <> ADP + Phosphate + SAICARR04591tRNA(Asp) + L-Aspartic acid + Adenosine triphosphate <> L-Aspartyl-tRNA(Asp) + Pyrophosphate + Adenosine monophosphateR05577a dipetide with aspartate at N-terminal + Water L-Aspartic acid + a standard α amino acid3.4.13.21-RXNL-Aspartic acid + Inosinic acid + Guanosine triphosphate > Hydrogen ion + adenylo-succinate + Phosphate + Guanosine diphosphateADENYLOSUCCINATE-SYNTHASE-RXNL-Aspartic acid + Citrulline + Adenosine triphosphate > Hydrogen ion + L-arginino-succinate + Pyrophosphate + Adenosine monophosphateARGSUCCINSYN-RXNAmmonia + L-Aspartic acid + Adenosine triphosphate > L-Asparagine + Pyrophosphate + Adenosine monophosphateR00483ASNSYNA-RXNL-Aspartic acid + Oxoglutaric acid <> Oxalacetic acid + L-GlutamateASPAMINOTRANS-RXNL-Asparagine + Water > Hydrogen ion + L-Aspartic acid + AmmoniaR00485ASPARAGHYD-RXNL-Aspartic acid <> Hydrogen ion + Fumaric acid + AmmoniaR00490ASPARTASE-RXNL-Aspartic acid + Adenosine triphosphate > L-Aspartyl-4-phosphate + ADPASPARTATEKIN-RXNL-Aspartic acid + Carbamoylphosphate > Hydrogen ion + Ureidosuccinic acid + PhosphateASPCARBTRANS-RXNHydrogen ion + L-Aspartic acid > beta-Alanine + Carbon dioxideASPDECARBOX-RXNOxygen + L-Aspartic acid > Hydrogen ion + Hydrogen peroxide + Iminoaspartic acidL-ASPARTATE-OXID-RXNPyridoxamine + Oxalacetic acid <> Pyridoxal + L-Aspartic acidPYROXALTRANSAM-RXNala-asp + Water > L-Alanine + L-Aspartic acidRXN0-6975gly-asp + Water > Glycine + L-Aspartic acidRXN0-6987Adenosine triphosphate + 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-Aspartic acid > Hydrogen ion + ADP + Phosphate + SAICARR04591SAICARSYN-RXNAdenosine triphosphate + L-Aspartic acid + Water > L-Aspartic acid + ADP + Phosphate + Hydrogen ionTRANS-RXN0-222Adenosine triphosphate + L-Aspartic acid + Water > L-Aspartic acid + ADP + Phosphate + Hydrogen ionTRANS-RXN0-222L-Aspartic acid + Oxoglutaric acid > Oxalacetic acid + L-GlutamateAdenosine triphosphate + L-Aspartic acid > ADP + L-4-aspartyl phosphateAdenosine triphosphate + L-Aspartic acid + L-Glutamine + Water > Adenosine monophosphate + Pyrophosphate + L-Asparagine + L-GlutamateL-Aspartic acid > Fumaric acid + AmmoniaL-Asparagine + Water > L-Aspartic acid + AmmoniaAdenosine triphosphate + Citrulline + L-Aspartic acid > Adenosine monophosphate + Pyrophosphate + 2-(N(omega)-L-arginino)succinateL-Aspartic acid + Oxygen > Iminoaspartic acid + Hydrogen peroxideL-Aspartic acid > beta-Alanine + Carbon dioxideAdenosine triphosphate + 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-Aspartic acid > ADP + Inorganic phosphate + SAICARGuanosine triphosphate + Inosinic acid + L-Aspartic acid > Guanosine diphosphate + Inorganic phosphate + N(6)-(1,2-dicarboxyethyl)AMPCarbamoylphosphate + L-Aspartic acid > Inorganic phosphate + Ureidosuccinic acidAdenosine triphosphate + L-Aspartic acid + tRNA(Asp) > Adenosine monophosphate + Pyrophosphate + L-aspartyl-tRNA(Asp)Adenosine triphosphate + L-Aspartic acid + L-Glutamine + Water + Ammonia <> Adenosine monophosphate + Pyrophosphate + L-Asparagine + L-GlutamateR00578 L-Aspartic acid + Adenosine triphosphate + L-Aspartic acid > Adenosine diphosphate + L-Aspartyl-4-phosphate + ADPPW_R002525Adenosine triphosphate + L-Aspartic acid + Ammonia + L-Aspartic acid > Adenosine monophosphate + L-Asparagine + Pyrophosphate + L-AsparaginePW_R002642Adenosine triphosphate + L-Aspartic acid + L-Glutamine + Water + L-Aspartic acid > Adenosine monophosphate + Pyrophosphate + L-Asparagine + L-Glutamic acid + L-Asparagine + L-GlutamatePW_R002643L-Aspartic acid + Oxoglutaric acid + L-Aspartic acid > Oxalacetic acid + L-Glutamic acid + L-GlutamatePW_R002644L-Glutamic acid + Oxalacetic acid + L-Glutamate > L-Aspartic acid + Oxoglutaric acid + L-Aspartic acidPW_R002667L-Aspartic acid + Water + Oxygen + L-Aspartic acid > Oxalacetic acid + Ammonia + Hydrogen peroxidePW_R002645L-Aspartic acid + Oxygen + L-Aspartic acid > Hydrogen peroxide + Hydrogen ion + Iminoaspartic acidPW_R003007L-Aspartic acid + L-Aspartic acid > Fumaric acid + AmmoniaPW_R002646L-Aspartic acid + L-Aspartic acid > Fumaric acid + AmmoniumPW_R002668Guanosine triphosphate + Inosinic acid + L-Aspartic acid + L-Aspartic acid > Guanosine diphosphate + Phosphate + N(6)-(1,2-dicarboxyethyl)AMPPW_R002648Inosinic acid + L-Aspartic acid + Guanosine triphosphate + L-Aspartic acid > Guanosine diphosphate + Phosphate +2 Hydrogen ion + N(6)-(1,2-dicarboxyethyl)AMP + Adenylsuccinic acidPW_R003424Adenosine triphosphate + Citrulline + L-Aspartic acid + L-Aspartic acid > Pyrophosphate + Adenosine monophosphate + Argininosuccinic acidPW_R002649L-Aspartic acid + L-Aspartic acid > N-carbamoyl-L-aspartatePW_R002650L-Aspartic acid + Adenosine triphosphate + Hydrogen ion + tRNA(Asp) + L-Aspartic acid > Pyrophosphate + Adenosine monophosphate + L-aspartyl-tRNA(Asp)PW_R002834L-Aspartic acid + Water + Adenosine triphosphate + L-Glutamine + L-Aspartic acid > L-Asparagine + Hydrogen ion + Adenosine monophosphate + L-Glutamic acid + Pyrophosphate + L-Asparagine + L-GlutamatePW_R002887L-Aspartic acid + Adenosine triphosphate + Ammonium + L-Aspartic acid > L-Asparagine + Adenosine monophosphate + Pyrophosphate + Hydrogen ion + L-AsparaginePW_R002888L-Aspartic acid + Hydrogen ion + L-Aspartic acid Carbon dioxide + beta-AlaninePW_R002998L-Aspartic acid + Hydrogen ion + L-Aspartic acid > Carbon dioxide + beta-AlaninePW_R003364L-Asparagine + Water + L-Asparagine > L-Aspartic acid + Ammonium + L-Aspartic acidPW_R0033885-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-Aspartic acid + Adenosine triphosphate + L-Aspartic acid > SAICAR + Phosphate + Adenosine diphosphate + Hydrogen ion + SAICAR + ADPPW_R003419Carbamoylphosphate + L-Aspartic acid + L-Aspartic acid > Phosphate + Hydrogen ion + N-carbamoyl-L-aspartatePW_R003526L-Aspartic acid + Adenosine triphosphate + Water + L-Aspartic acid > Adenosine diphosphate + Phosphate + Hydrogen ion + L-Aspartic acid + ADPPW_RCT000108L-Aspartic acid + Carbamoylphosphate <> Ureidosuccinic acid + Hydrogen ion + PhosphateL-Aspartic acid + Oxygen <> Hydrogen ion + Hydrogen peroxide + Iminoaspartic acidL-Aspartic acid + Adenosine triphosphate <> L-Aspartyl-4-phosphate + ADPL-Aspartic acid + Adenosine triphosphate + tRNA(Asp) <> Adenosine monophosphate + L-Aspartyl-tRNA(Asp) + Pyrophosphate5 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-Aspartic acid + Adenosine triphosphate <> SAICAR + ADP + Hydrogen ion + PhosphateL-Asparagine + Water <> L-Aspartic acid + AmmoniaL-Aspartic acid + Adenosine triphosphate + Citrulline <> Adenosine monophosphate + Argininosuccinic acid + Hydrogen ion + PyrophosphateL-Aspartic acid + Hydrogen ion <> beta-Alanine + Carbon dioxideL-Aspartic acid + Guanosine triphosphate + Inosinic acid <> Adenylsuccinic acid + Guanosine diphosphate +2 Hydrogen ion + PhosphateL-Aspartic acid <> Fumaric acid + AmmoniaL-Aspartic acid <> Hydrogen ion + Fumaric acid + AmmoniaL-Aspartic acid + Carbamoylphosphate <> Ureidosuccinic acid + Hydrogen ion + PhosphateL-Aspartic acid + Oxygen <> Hydrogen ion + Hydrogen peroxide + Iminoaspartic acid5 5-Amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate + L-Aspartic acid + Adenosine triphosphate <> SAICAR + ADP + Hydrogen ion + PhosphateL-Asparagine + Water > Hydrogen ion + L-Aspartic acid + AmmoniaL-Aspartic acid + Adenosine triphosphate + Citrulline <> Adenosine monophosphate + Argininosuccinic acid + Hydrogen ion + PyrophosphateGutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glucoseShake flask and filter culture4230.0uM0.037 oCK12 NCM3722Mid-Log Phase169200000Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.19561621Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L glycerolShake flask and filter culture9300.0uM0.037 oCK12 NCM3722Mid-Log Phase372000000Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.19561621Gutnick minimal complete medium (4.7 g/L KH2PO4; 13.5 g/L K2HPO4; 1 g/L K2SO4; 0.1 g/L MgSO4-7H2O; 10 mM NH4Cl) with 4 g/L acetateShake flask and filter culture7350.0uM0.037 oCK12 NCM3722Mid-Log Phase294000000Bennett, B. D., Kimball, E. H., Gao, M., Osterhout, R., Van Dien, S. J., Rabinowitz, J. D. (2009). "Absolute metabolite concentrations and implied enzyme active site occupancy in Escherichia coli." Nat Chem Biol 5:593-599.1956162148 mM Na2HPO4, 22 mM KH2PO4, 10 mM NaCl, 45 mM (NH4)2SO4, supplemented with 1 mM MgSO4, 1 mg/l thiamine·HCl, 5.6 mg/l CaCl2, 8 mg/l FeCl3, 1 mg/l MnCl2·4H2O, 1.7 mg/l ZnCl2, 0.43 mg/l CuCl2·2H2O, 0.6 mg/l CoCl2·2H2O and 0.6 mg/l Na2MoO4·2H2O. 4 g/L GlucoBioreactor, pH controlled, O2 and CO2 controlled, dilution rate: 0.2/h337.0uM0.037 oCBW25113Stationary Phase, glucose limited13480000Ishii, N., Nakahigashi, K., Baba, T., Robert, M., Soga, T., Kanai, A., Hirasawa, T., Naba, M., Hirai, K., Hoque, A., Ho, P. Y., Kakazu, Y., Sugawara, K., Igarashi, S., Harada, S., Masuda, T., Sugiyama, N., Togashi, T., Hasegawa, M., Takai, Y., Yugi, K., Arakawa, K., Iwata, N., Toya, Y., Nakayama, Y., Nishioka, T., Shimizu, K., Mori, H., Tomita, M. (2007). "Multiple high-throughput analyses monitor the response of E. coli to perturbations." Science 316:593-597.17379776Luria-Bertani (LB) mediaShake flask662.0uMtrue45.037 oCBL21 DE3Stationary phase cultures (overnight culture)2648000180000Lin, Z., Johnson, L. C., Weissbach, H., Brot, N., Lively, M. O., Lowther, W. T. (2007). "Free methionine-(R)-sulfoxide reductase from Escherichia coli reveals a new GAF domain function." Proc Natl Acad Sci U S A 104:9597-9602.17535911